Abstract
WISp39 and Hsp90: actin' together in cell migration.
Highlights
Cell motility is an actin dependent process requiring the formation and extension of lamellipodia or filopodia, and is absolutely essential for many cellular processes, especially for morphogenesis during development
What is known is that Arp2/3 dependent actin assembly and Cofilin dependent disassembly are coordinately regulated at the leading edge by Coronin 1B, which binds the Arp2/3 complex in a phosphorylationdependent manner
We have found that WISp39 (Waf1 Cip1 stabilizing protein 39), an Hsp90 binding www.impactjournals.com/oncotarget protein we had discovered [4], coordinates Coronin 1B, Arp2/3 complex and Cofilin activity in the lamellipodia to achieve directed cell motility [5]
Summary
Cell motility is an actin dependent process requiring the formation and extension of lamellipodia or filopodia, and is absolutely essential for many cellular processes, especially for morphogenesis during development. What is known is that Arp2/3 dependent actin assembly and Cofilin dependent disassembly are coordinately regulated at the leading edge by Coronin 1B, which binds the Arp2/3 complex in a phosphorylationdependent manner. The regulation of phosphorylated Coronin 1B is essential to control Arp2/3 complex activity and the rate of actin nucleation and branching at the leading edge.
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